ID   Q9UFN8_HUMAN            Unreviewed;       270 AA.
AC   Q9UFN8;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   SubName: Full=Uncharacterized protein DKFZp434G162 {ECO:0000313|EMBL:CAB55983.1};
DE   Flags: Fragment;
GN   Name=DKFZp434G162 {ECO:0000313|EMBL:CAB55983.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:CAB55983.1};
RN   [1] {ECO:0000313|EMBL:CAB55983.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Testis {ECO:0000313|EMBL:CAB55983.1};
RG   The German cDNA Consortium;
RA   Ansorge W., Krieger S., Regiert T., Rittmueller C., Schwager B.,
RA   Mewes H.W., Weil B., Amid C., Osanger A., Fobo G., Han M., Wiemann S.;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC       {ECO:0000256|ARBA:ARBA00004246}.
CC   -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC       {ECO:0000256|ARBA:ARBA00007881}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL117537; CAB55983.1; -; mRNA.
DR   PIR; T17293; T17293.
DR   AlphaFoldDB; Q9UFN8; -.
DR   PeptideAtlas; Q9UFN8; -.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   CDD; cd01213; PTB_tensin; 1.
DR   CDD; cd09927; SH2_Tensin_like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR035012; Tensin-like_SH2.
DR   InterPro; IPR033929; Tensin_PTB.
DR   PANTHER; PTHR45734; TENSIN; 1.
DR   PANTHER; PTHR45734:SF3; TENSIN-1; 1.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF00017; SH2; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191}.
FT   DOMAIN          1..107
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAB55983.1"
SQ   SEQUENCE   270 AA;  29353 MW;  44F96278ACCB5D8C CRC64;
     PEISREQAIA LLKDQEPGAF IIRDSHSFRG AYGLAMKVSS PPPTIMQQNK KGDMTHELVR
     HFLIETGPRG VKLKGCPNEP NFGSLSALVY QHSIIPLALP CKLVIPNRDP TDESKDSSGP
     ANSTADLLKQ GAACNVLFVN SVDMESLTGP QAISKATSET LAADPTPAAT IVHFKVSAQG
     ITLTDNQRKL FFRRHYPLNT VTFCDLDPQE RKWMKTEGGA PAKLFGFVAR KQGSTTDNAC
     HLFAELDPNQ PASAIVNFVS KVMLNAGQKR
//